ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Telomere zinc finger-associated protein

Intramolecular
Cysteine 286 and cysteine 289
Cysteine 373 and cysteine 376
Cysteine 345 and cysteine 348
Cysteine 314 and cysteine 317
Cysteine 314 and cysteine 335
Cysteine 317 and cysteine 335
Cysteine 46 and cysteine 47
Cysteine 317 and cysteine 320
Cysteine 314 and cysteine 320
Cysteine 289 and cysteine 320
A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 286 and 289 (10 and 13 respectively in this structure).

Details

Redox score ?
91
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q99K15
Residue number A
286
Residue number B
289
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 286 of Telomere zinc finger-associated protein

Cysteine 289 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 373 and 376 (97 and 100 respectively in this structure).

Details

Redox score ?
87
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q99K15
Residue number A
373
Residue number B
376
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 373 of Telomere zinc finger-associated protein

Cysteine 376 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 345 and 348 (69 and 72 respectively in this structure).

Details

Redox score ?
85
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
Q99K15
Residue number A
345
Residue number B
348
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 345 of Telomere zinc finger-associated protein

Cysteine 348 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 314 and 317 (38 and 41 respectively in this structure).

Details

Redox score ?
85
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
1
Peptide accession
Q99K15
Residue number A
314
Residue number B
317
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 314 of Telomere zinc finger-associated protein

Cysteine 317 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 314 and 335 (38 and 59 respectively in this structure).

Details

Redox score ?
85
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
0
Peptide accession
Q99K15
Residue number A
314
Residue number B
335
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 314 of Telomere zinc finger-associated protein

Cysteine 335 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 317 and 335 (41 and 59 respectively in this structure).

Details

Redox score ?
84
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
1
Peptide accession
Q99K15
Residue number A
317
Residue number B
335
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 317 of Telomere zinc finger-associated protein

Cysteine 335 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 46 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3b84
Structure name
crystal structure of the human btb domain of the krueppel related zinc finger protein 3 (hkr3)
Structure deposition date
2007-10-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10074
Residue number A
46
Residue number B
47
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 46 of Telomere zinc finger-associated protein

Cysteine 47 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 317 and 320 (41 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
4
Peptide accession
Q99K15
Residue number A
317
Residue number B
320
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 317 of Telomere zinc finger-associated protein

Cysteine 320 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 314 and 320 (38 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
2
Peptide accession
Q99K15
Residue number A
314
Residue number B
320
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 314 of Telomere zinc finger-associated protein

Cysteine 320 of Telomere zinc finger-associated protein

A redox-regulated disulphide may form within Telomere zinc finger-associated protein between cysteines 289 and 320 (13 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2dlq
Structure name
solution structure of the tandem four zf-c2h2 domain repeats of murine gli-kruppel family member hkr3
Structure deposition date
2006-04-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
3
Peptide accession
Q99K15
Residue number A
289
Residue number B
320
Peptide name
Telomere zinc finger-associated protein

Ligandability

Cysteine 289 of Telomere zinc finger-associated protein

Cysteine 320 of Telomere zinc finger-associated protein

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